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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The N Terminus of the <italic>Escherichia coli</italic> Transcription Activator MalT Is the Domain of Interaction with MalY</title><author><name sortKey="Schlegel, Anja" sort="Schlegel, Anja" uniqKey="Schlegel A" first="Anja" last="Schlegel">Anja Schlegel</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Danot, Olivier" sort="Danot, Olivier" uniqKey="Danot O" first="Olivier" last="Danot">Olivier Danot</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Richet, Evelyne" sort="Richet, Evelyne" uniqKey="Richet E" first="Evelyne" last="Richet">Evelyne Richet</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Ferenci, Thomas" sort="Ferenci, Thomas" uniqKey="Ferenci T" first="Thomas" last="Ferenci">Thomas Ferenci</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Boos, Winfried" sort="Boos, Winfried" uniqKey="Boos W" first="Winfried" last="Boos">Winfried Boos</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12003949</idno><idno type="pmc">135079</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC135079</idno><idno type="RBID">PMC:135079</idno><idno type="doi">10.1128/JB.184.11.3069-3077.2002</idno><date when="2002">2002</date><idno type="wicri:Area/Pmc/Corpus">000F99</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000F99</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The N Terminus of the <italic>Escherichia coli</italic> Transcription Activator MalT Is the Domain of Interaction with MalY</title><author><name sortKey="Schlegel, Anja" sort="Schlegel, Anja" uniqKey="Schlegel A" first="Anja" last="Schlegel">Anja Schlegel</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Danot, Olivier" sort="Danot, Olivier" uniqKey="Danot O" first="Olivier" last="Danot">Olivier Danot</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Richet, Evelyne" sort="Richet, Evelyne" uniqKey="Richet E" first="Evelyne" last="Richet">Evelyne Richet</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Ferenci, Thomas" sort="Ferenci, Thomas" uniqKey="Ferenci T" first="Thomas" last="Ferenci">Thomas Ferenci</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Boos, Winfried" sort="Boos, Winfried" uniqKey="Boos W" first="Winfried" last="Boos">Winfried Boos</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="2002">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The maltose system of <italic>Escherichia coli</italic> consists of a number of genes encoding proteins involved in the uptake and metabolism of maltose and maltodextrins. The system is positively regulated by MalT, its transcriptional activator. MalT activity is controlled by two regulatory circuits: a positive one with maltotriose as effector and a negative one involving several proteins. MalK, the ATP-hydrolyzing subunit of the cognate ABC transporter, MalY, an enzyme with the activity of a cystathionase, and Aes, an acetyl esterase, phenotypically act as repressors of MalT activity. By in vivo titration assays, we have shown that the N-terminal 250 amino acids of MalT contain the interaction site for MalY but not for MalK. This was confirmed by gel filtration analysis, where MalY was shown to coelute with the N-terminal MalT structural domain. Mutants in MalT causing elevated <italic>mal</italic> gene expression in the absence of exogenous maltodextrins were tested in their response to the three repressors. The different MalT mutations exhibited a various degree of sensitivity towards these repressors, but none was resistant to all of them. Some of them became nearly completely resistant to Aes while still being sensitive to MalY. These mutations are located at positions 38, 220, 243, and 359, most likely defining the interaction patch with Aes on the three-dimensional structure of MalT.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id><journal-id journal-id-type="publisher-id">jb</journal-id><journal-title>Journal of Bacteriology</journal-title><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12003949</article-id><article-id pub-id-type="pmc">135079</article-id><article-id pub-id-type="publisher-id">1591</article-id><article-id pub-id-type="doi">10.1128/JB.184.11.3069-3077.2002</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymes and Proteins</subject></subj-group></article-categories><title-group><article-title>The N Terminus of the <italic>Escherichia coli</italic> Transcription Activator MalT Is the Domain of Interaction with MalY</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Schlegel</surname><given-names>Anja</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Danot</surname><given-names>Olivier</given-names></name><xref ref-type="aff" rid="aff1">2</xref></contrib><contrib contrib-type="author"><name><surname>Richet</surname><given-names>Evelyne</given-names></name><xref ref-type="aff" rid="aff1">2</xref></contrib><contrib contrib-type="author"><name><surname>Ferenci</surname><given-names>Thomas</given-names></name><xref ref-type="aff" rid="aff1">3</xref></contrib><contrib contrib-type="author"><name><surname>Boos</surname><given-names>Winfried</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff1">Department of Biology, University of Konstanz, 78457 Konstanz, Germany,<label>1</label> Unité de Génétique Moléculaire, Institut Pasteur, FRE CNRS 2364, 75724 Paris Cedex 15, France,<label>2</label> Department of Microbiology G08, University of Sydney, Sydney, New South Wales 2006, Australia<label>3</label></aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address: Department of Biology, University of Konstanz, Konstanz, Germany. Phone: 49 7531 882658. Fax: 49 7531 883356. E-mail: <email>Winfried.Boos@uni-konstanz.de</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>6</month><year>2002</year></pub-date><volume>184</volume><issue>11</issue><fpage>3069</fpage><lpage>3077</lpage><history><date date-type="received"><day>26</day><month>12</month><year>2001</year></date><date date-type="accepted"><day>1</day><month>3</month><year>2002</year></date></history><copyright-statement>Copyright © 2002, American Society for Microbiology</copyright-statement><copyright-year>2002</copyright-year><abstract><p>The maltose system of <italic>Escherichia coli</italic> consists of a number of genes encoding proteins involved in the uptake and metabolism of maltose and maltodextrins. The system is positively regulated by MalT, its transcriptional activator. MalT activity is controlled by two regulatory circuits: a positive one with maltotriose as effector and a negative one involving several proteins. MalK, the ATP-hydrolyzing subunit of the cognate ABC transporter, MalY, an enzyme with the activity of a cystathionase, and Aes, an acetyl esterase, phenotypically act as repressors of MalT activity. By in vivo titration assays, we have shown that the N-terminal 250 amino acids of MalT contain the interaction site for MalY but not for MalK. This was confirmed by gel filtration analysis, where MalY was shown to coelute with the N-terminal MalT structural domain. Mutants in MalT causing elevated <italic>mal</italic> gene expression in the absence of exogenous maltodextrins were tested in their response to the three repressors. The different MalT mutations exhibited a various degree of sensitivity towards these repressors, but none was resistant to all of them. Some of them became nearly completely resistant to Aes while still being sensitive to MalY. These mutations are located at positions 38, 220, 243, and 359, most likely defining the interaction patch with Aes on the three-dimensional structure of MalT.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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